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Arch Biochem Biophys. 2012 Jul 15;523(2):144-50. doi: 10.1016/j.abb.2012.04.021. Epub 2012 May 3.

Trehalose inhibits fibrillation of A53T mutant alpha-synuclein and disaggregates existing fibrils.

Author information

1
Department of Neurology, Huashan Hospital, Fudan University, Shanghai 200040, China.

Abstract

The aggregation of alpha-synuclein (AS) is pivotally implicated in the development of Parkinson's disease (PD), inhibiting this process might be effective in treating PD. Here, by using circular dichroism spectroscopy, thioflavin T fluorescence, and atomic force microscopy, we found that trehalose at low concentration disaggregates preformed A53T AS protofibrils and fibrils into small aggregates or even random coil structure, while trehalose at high concentration slows down the structural transition into β-sheet structure and completely prevents the formation of mature A53T AS fibrils. Further work in vivo will be needed to evaluate its potential as a novel strategy for treating PD.

PMID:
22575388
DOI:
10.1016/j.abb.2012.04.021
[Indexed for MEDLINE]

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